VE-cadherin shedding in vitro and in patients with aortic aneurysm and dissection.

VE-cadherin (VEC) is a major endothelial adhesion protein, which controls vascular homeostasis. During vascular diseases, VEC can be shed from the endothelial surface by proteases like ADAM10/17, which cleave the extracellular domain of VEC in response to inflammatory cytokines like TNF-α. The resulting, soluble fragments (sVEC) are discussed as a potential marker for endothelial barrier breakdown.

The short-chain fatty acid butyrate exerts a specific effect on VE-cadherin phosphorylation and alters the integrity of aortic endothelial cells.

Short-chain fatty acids (SCFAs) like butyrate (BUT) largely influence vascular integrity and are closely associated with the onset and progression of cardiovascular diseases. However, their impact on vascular endothelial cadherin (VEC), a major vascular adhesion and signaling molecule, is largely unknown. Here, we explored the effect of the SCFA BUT on the phosphorylation of specific tyrosine residues of VEC (Y731, Y685, and Y658), which are reported to be critical for VEC regulation and vascular integrity.